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Volumn 9, Issue 7, 2000, Pages 1382-1390

HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold

Author keywords

Adhesion; Complement control protein; Fibronectin type III; Hyalin; Hydrophobic cluster analysis; Iterative database search; Polycystic kidney disease

Indexed keywords

BACTERIAL PROTEIN; CHITINASE; FIBRONECTIN; IMMUNOGLOBULIN;

EID: 0033854828     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.7.1382     Document Type: Article
Times cited : (61)

References (39)
  • 1
    • 0031793928 scopus 로고    scopus 로고
    • Iterated profile searches with PSI-BLAST - A tool for discovery in protein databases
    • Altschul SF, Koonin EV. 1998. Iterated profile searches with PSI-BLAST - A tool for discovery in protein databases. Trends Biochem Sci 23:444-447.
    • (1998) Trends Biochem Sci , vol.23 , pp. 444-447
    • Altschul, S.F.1    Koonin, E.V.2
  • 6
    • 0028774038 scopus 로고
    • Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution
    • Bodian DL, Jones EY, Harlos K, Stuart DI, Davis SI. 1994. Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution. Structure 2:755-766.
    • (1994) Structure , vol.2 , pp. 755-766
    • Bodian, D.L.1    Jones, E.Y.2    Harlos, K.3    Stuart, D.I.4    Davis, S.I.5
  • 7
    • 0003338119 scopus 로고
    • A proposed nomenclature for the extracellular protein modules of animals
    • Poster CO2
    • Bork P, Bairoch A. 1995. A proposed nomenclature for the extracellular protein modules of animals. Trends Biochem Sci 20(3): Poster CO2.
    • (1995) Trends Biochem Sci , vol.20 , Issue.3
    • Bork, P.1    Bairoch, A.2
  • 8
    • 0026644395 scopus 로고
    • Proposed acquisition of an animal protein domain by bacteria
    • Bork P. Doolittle RF. 1992. Proposed acquisition of an animal protein domain by bacteria. Proc Natl Acad Sci USA 89:8990-8994.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8990-8994
    • Bork, P.1    Doolittle, R.F.2
  • 9
    • 0029777325 scopus 로고    scopus 로고
    • Structure and distribution of modules in extracellular proteins
    • Bork P, Downing AK, Kieffer B, Campbell ID. 1996. Structure and distribution of modules in extracellular proteins. Q Rev Biophys 19:119-167.
    • (1996) Q Rev Biophys , vol.19 , pp. 119-167
    • Bork, P.1    Downing, A.K.2    Kieffer, B.3    Campbell, I.D.4
  • 10
    • 0028172534 scopus 로고
    • The immunoglobulin fold. Structural classification, sequence patterns and common core
    • Bork P, Holm L, Sander C. 1994. The immunoglobulin fold. Structural classification, sequence patterns and common core. J Mol Biol 242:309-320.
    • (1994) J Mol Biol , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 11
  • 12
    • 0032991918 scopus 로고    scopus 로고
    • The BAH (Bromo-Adjacent Homology) domain: A link between methylation, replication and transcriptional regulation
    • Callebaut I, Courvalin JC, Mornon JP. 1999. The BAH (Bromo-Adjacent Homology) domain: A link between methylation, replication and transcriptional regulation. FEBS Lett 446:189-193.
    • (1999) FEBS Lett , vol.446 , pp. 189-193
    • Callebaut, I.1    Courvalin, J.C.2    Mornon, J.P.3
  • 14
    • 0028773478 scopus 로고
    • Building proteins with fibronectin type III modules
    • Campbell ID, Spitzfaden C. 1994. Building proteins with fibronectin type III modules. Structure 2:333-337.
    • (1994) Structure , vol.2 , pp. 333-337
    • Campbell, I.D.1    Spitzfaden, C.2
  • 17
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy SR. 1998. Profile hidden Markov models. Bioinformatics 14:755-763.
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 18
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Metoz F. 1999. ESPript: Analysis of multiple sequence alignments in PostScript. Bioinformatics 15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 19
    • 0032773506 scopus 로고    scopus 로고
    • The immunoglobulin fold family: Sequence analysis and 3D structure comparisons
    • Halaby DM, Poupon A, Mornon JP. 1999. The immunoglobulin fold family: Sequence analysis and 3D structure comparisons. Protein Eng 12:563-571.
    • (1999) Protein Eng , vol.12 , pp. 563-571
    • Halaby, D.M.1    Poupon, A.2    Mornon, J.P.3
  • 20
    • 0028361540 scopus 로고
    • Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains
    • Harpaz Y. Chotia C. 1994. Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J Mol Biol 238: 528-539.
    • (1994) J Mol Biol , vol.238 , pp. 528-539
    • Harpaz, Y.1    Chotia, C.2
  • 22
    • 0028351169 scopus 로고
    • Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 Å
    • Huber AH, Wang YM, Bieber AJ, Bjorkman PJ. 1994. Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 Å. Neuron 12:717-731.
    • (1994) Neuron , vol.12 , pp. 717-731
    • Huber, A.H.1    Wang, Y.M.2    Bieber, A.J.3    Bjorkman, P.J.4
  • 23
    • 0030272010 scopus 로고    scopus 로고
    • Three-dimensional structure of cell adhesion molecules
    • Jones EY. 1996. Three-dimensional structure of cell adhesion molecules. Curr Opin Cell Biol 8:602-608.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 602-608
    • Jones, E.Y.1
  • 25
    • 0000243829 scopus 로고
    • Molscript - A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. Molscript - A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 12:283-291.
    • (1991) J Appl Crystallogr , vol.12 , pp. 283-291
    • Kraulis, P.J.1
  • 26
    • 0026490256 scopus 로고
    • Structure of a fibronectin lype III domain from tenascin phased by MAD analysis of selenomethyionyl protein
    • Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP. 1992. Structure of a fibronectin lype III domain from tenascin phased by MAD analysis of selenomethyionyl protein. Science 258:987-991.
    • (1992) Science , vol.258 , pp. 987-991
    • Leahy, D.J.1    Hendrickson, W.A.2    Aukhil, I.3    Erickson, H.P.4
  • 27
    • 0027943212 scopus 로고
    • Tracing the spread of fibronectin type III domains in bacterial glycohydrolases
    • Little E, Bork P, Doolittle RF. 1994. Tracing the spread of fibronectin type III domains in bacterial glycohydrolases. J Mol Evol 39:631-643.
    • (1994) J Mol Evol , vol.39 , pp. 631-643
    • Little, E.1    Bork, P.2    Doolittle, R.F.3
  • 29
    • 0028956981 scopus 로고
    • Solution structure of the epithelial cadherin domain responsible for selective cell adhesion
    • Overduin M, Harvey TS, Bagby S, Tong KI, Yau P, Takeichi M, Ikura M. 1995. Solution structure of the epithelial cadherin domain responsible for selective cell adhesion. Science 267:386-389.
    • (1995) Science , vol.267 , pp. 386-389
    • Overduin, M.1    Harvey, T.S.2    Bagby, S.3    Tong, K.I.4    Yau, P.5    Takeichi, M.6    Ikura, M.7
  • 30
    • 0032919370 scopus 로고    scopus 로고
    • SMART: Identification and annotation of domains from signalling and extracellular protein sequences
    • Ponting CP, Schultz J, Milpetz F, Bork P. 1999. SMART: Identification and annotation of domains from signalling and extracellular protein sequences. Nucleic Acids Res 27:229-232.
    • (1999) Nucleic Acids Res , vol.27 , pp. 229-232
    • Ponting, C.P.1    Schultz, J.2    Milpetz, F.3    Bork, P.4
  • 31
    • 0024561914 scopus 로고
    • Structure-function relationships of the complement components
    • Reid KBM, Day AJ. 1989. Structure-function relationships of the complement components. Immunol Today 6:177-180.
    • (1989) Immunol Today , vol.6 , pp. 177-180
    • Reid, K.B.M.1    Day, A.J.2
  • 33
    • 0032918222 scopus 로고    scopus 로고
    • Infectionderived Enterococcus faecalis strains are enriched in esp. a gene encoding a novel surface protein
    • Shankar V, Baghdayan AS, Huycke MM, Lindahl G, Gilmore MS. 1999. Infectionderived Enterococcus faecalis strains are enriched in esp. a gene encoding a novel surface protein. Infect Immun 67:193-200.
    • (1999) Infect Immun , vol.67 , pp. 193-200
    • Shankar, V.1    Baghdayan, A.S.2    Huycke, M.M.3    Lindahl, G.4    Gilmore, M.S.5
  • 36
    • 0345279861 scopus 로고    scopus 로고
    • The R28 protein of Streptococcus pyogenes is related to several group B streptococcal surface proteins, confers protective immunity and promotes binding to human epithelial cells
    • Stalhammar-Carlemalm M, Areschoug T, Larsson C, Lindahl G. 1999. The R28 protein of Streptococcus pyogenes is related to several group B streptococcal surface proteins, confers protective immunity and promotes binding to human epithelial cells. Mol Microbiol 33:208-219.
    • (1999) Mol Microbiol , vol.33 , pp. 208-219
    • Stalhammar-Carlemalm, M.1    Areschoug, T.2    Larsson, C.3    Lindahl, G.4
  • 37
    • 0033229842 scopus 로고    scopus 로고
    • The third chitinase gene (chiC) of Serratia marcescens 170 and the relationship of its product to other bacterial chitinases
    • Suzuki K, Taiyoji M, Sugawara N, Nikaidou N, Henrissat B, Watanabe T. 1999. The third chitinase gene (chiC) of Serratia marcescens 170 and the relationship of its product to other bacterial chitinases. Biochem J 343:587-596.
    • (1999) Biochem J , vol.343 , pp. 587-596
    • Suzuki, K.1    Taiyoji, M.2    Sugawara, N.3    Nikaidou, N.4    Henrissat, B.5    Watanabe, T.6
  • 38
    • 0029763036 scopus 로고    scopus 로고
    • Identification of a family of streptococcal surface proteins with extremely repetitive structure
    • Wästfelt M. Stälhammar-Carlemalm M, Delisse AM, Cabezon T, Lindahl G. 1996. Identification of a family of streptococcal surface proteins with extremely repetitive structure. J Biol Chem 271:18892-18897.
    • (1996) J Biol Chem , vol.271 , pp. 18892-18897
    • Wästfelt, M.1    Stälhammar-Carlemalm, M.2    Delisse, A.M.3    Cabezon, T.4    Lindahl, G.5
  • 39
    • 0032518438 scopus 로고    scopus 로고
    • A molecular analysis of hyalin, a substrate for cell adhesion in the hyaline layer of the sea urchin embryo
    • Wessel G, Berg L, Adelson DL, Cannon G, McClay DR. 1998. A molecular analysis of hyalin, a substrate for cell adhesion in the hyaline layer of the sea urchin embryo. Dev Biol 193:115-126.
    • (1998) Dev Biol , vol.193 , pp. 115-126
    • Wessel, G.1    Berg, L.2    Adelson, D.L.3    Cannon, G.4    McClay, D.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.